Solution structure of omega-conotoxin mviic, a high affinity of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis. Determined by solution NMR. Released 1 Dec 1995.
Explore 1OMN in 3D Show helices and sheets RCSB PDB PDBe
1OMN contains 1 α-helix and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| α-helix | 10-12 | 3 | |
| β-strand | 25 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Omega-conotoxin M VII C (M seven C) | A | protein | 27 | Conus magus | P37300 (AlphaFold model) |
>1OMN_1 OMEGA-CONOTOXIN M VII C (M SEVEN C) (chains A) CKGKGAPCRKTMYDCCSGSCGRRGKCX
Solution structure of omega-conotoxin MVIIC, a high affinity ligand of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis. Farr-Jones, S., Miljanich, G.P., Nadasdi, L. et al. J Mol Biol (1995) 248:106-124. DOI 10.1006/jmbi.1995.0205 · PubMed
Other PDB entries of the same protein (UniProt P37300 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1OMN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.